Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Generalization of distance to higher dimensional objects.

Literature DB >> 17848528

Generalization of distance to higher dimensional objects.

Abstract

The measurement of distance between two objects is generalized to the case where the objects are no longer points but are one-dimensional. Additional concepts such as nonextensibility, curvature constraints, and noncrossing become central to the notion of distance. Analytical and numerical results are given for some specific examples, and applications to biopolymers are discussed.

Mesh：

Substances：
Biopolymers

Year: 2007 PMID： 17848528 PMCID： PMC1986585 DOI： 10.1073/pnas.0607833104

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

4 in total

1. Protein folding funnels: a kinetic approach to the sequence-structure relationship.

Authors: P E Leopold; M Montal; J N Onuchic
Journal: Proc Natl Acad Sci U S A Date: 1992-09-15 Impact factor: 11.205

2. P versus Q: structural reaction coordinates capture protein folding on smooth landscapes.

Authors: Samuel S Cho; Yaakov Levy; Peter G Wolynes
Journal: Proc Natl Acad Sci U S A Date: 2006-01-09 Impact factor: 11.205

3. A surface of minimum area metric for the structural comparison of proteins.

Authors: A Falicov; F E Cohen
Journal: J Mol Biol Date: 1996-05-24 Impact factor: 5.469

4. Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties.

Authors: T Veitshans; D Klimov; D Thirumalai
Journal: Fold Des Date: 1997

4 in total

3 in total

Generalization of distance to higher dimensional objects.

1. Protein folding funnels: a kinetic approach to the sequence-structure relationship.

2. P versus Q: structural reaction coordinates capture protein folding on smooth landscapes.

3. A surface of minimum area metric for the structural comparison of proteins.

4. Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties.

1. Minimal folding pathways for coarse-grained biopolymer fragments.

2. Minimum action principle and shape dynamics.

3. Polymer uncrossing and knotting in protein folding, and their role in minimal folding pathways.